ArticleProceedings of the National Academy of Sciences of the United States of America2003
Developing an energy landscape for the novel function of a (beta/alpha)8 barrel: ammonia conduction through HisF.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 50 citations in OpenAlex.
- Allosteric regulation of substrate channeling:Frontiers in molecular biosciences · 2022Review
- Solution NMR Spectroscopy for the Study of Enzyme Allostery.Chemical reviews · 2016Review
- Visualizing the tunnel in tryptophan synthase with crystallography: Insights into a selective filter for accommodating indole and rejecting water.Biochimica et biophysica acta · 2016Article
- Computational Studies of Molecular Permeation through Connexin26 Channels.Biophysical journal · 2016Article
- Capture and quality control mechanisms for adenosine-5'-triphosphate binding.Journal of the American Chemical Society · 2013Article
- Back to the future: can physical models of passive membrane permeability help reduce drug candidate attrition and move us beyond QSPR?Chemical biology & drug design · 2013Review
- Exploring residue component contributions to dynamical network models of allostery.Journal of chemical theory and computation · 2012Article
- Identification of genes involved in the acetamidino group modification of the flagellin N-linked glycan of Methanococcus maripaludis.Journal of bacteriology · 2012Article
- The interaction of ammonia and xenon with the imidazole glycerol phosphate synthase from Thermotoga maritima as detected by NMR spectroscopy.Protein science : a publication of the Protein Society · 2010Article
- Ligand escape pathways and (un)binding free energy calculations for the hexameric insulin-phenol complex.Biophysical journal · 2008Article
- The aldo-keto reductase superfamily and its role in drug metabolism and detoxification.Drug metabolism reviews · 2008Review
- Potentials of mean force for acetylcholine unbinding from the alpha7 nicotinic acetylcholine receptor ligand-binding domain.Journal of the American Chemical Society · 2006Article
- Structural elements in IGP synthase exclude water to optimize ammonia transfer.Biophysical journal · 2005Article
- Structural and genetic characterization of enterohemorrhagic Escherichia coli O145 O antigen and development of an O145 serogroup-specific PCR assay.Journal of bacteriology · 2005Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
HisH-hisF is a multidomain globular protein complex; hisH is a class I glutamine amidotransferase that hydrolyzes glutamine to form ammonia, and hisF is a (beta/alpha)8 barrel cyclase that completes the ring formation of imidizole glycerol phosphate synthase. Together, hisH and hisF form a glutamine amidotransferase that carries out the fifth step of the histidine biosynthetic pathway. Recently, it has been suggested that the (beta/alpha)8 barrel participates in a novel function: to channel ammonia from the active site of hisH to the active site of hisF. The present study presents a series of molecular dynamic simulations that investigate the channeling function of hisF. This article reconstructs potentials of mean force for the conduction of ammonia through the channel, and the entrance of ammonia through the strictly conserved channel gate, in both a closed and a hypothetical open conformation. The resulting energy landscape within the channel supports the idea that ammonia does indeed pass through the barrel, interacting with conserved hydrophilic residues along the way. The proposed open conformation, which involves an alternate rotamer state of one of the gate residues, presents only an approximately 2.5-kcal energy barrier to ammonia entry. Another alternate open-gate conformation, which may play a role in non-nitrogen-fixing organisms, is deduced through bioinformatics.
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